In recent years, it has been revealed that modification such as methylation or acetylation of a specific amino acid residue in a core histone protein causes a change in chromosomal chromatin structure, which plays an important role in gene regulation. Lysine-specific histone demethylase 1 (LSD1) is a histone demethylase that catalyses demethylation reactions of monomethylated lysine 4 (H3K4me1) and dimethylated lysine 4 (H3K4me2) of a core histone protein histone H3 (Non Patent Literature 1).
It has been reported that cell growth of cancer cells is suppressed by suppressing a function of LSD1 with RNAi. It has also been reported that use of trans-2-phenylcyclopropylamine to be described later as an LSD1 inhibitor is effective for treatment of leukemia.
trans-2-Phenylcyclopropylamine (tranylcypromine) and nialamide are known as compounds capable of inhibiting a function of LSD1 (Non Patent Literatures 1 and 2). However, each of those compounds is a compound that has low inhibitory activity against LSD1 and also inhibits monoamine oxidases (MAOs), which have high homology to LSD1, and hence is not an LSD1-selective inhibitor. MAOs (MAO-A and MAO-B in humans) are important in adjustment of a neurotransmitter, and hence it is difficult to clinically apply tranylcypromine or nialamide as the LSD1 inhibitor because of a high risk of side effects.
In Patent Literature 1 and Non Patent Literature 3, there is a disclosure of a phenylcyclopropylamine derivative capable of selectively inhibiting a function of LSD1. However, the compound has high selectivity for LSD1 but is insufficient in LSD1 inhibitory activity and in suppressing activity against cell growth of cancer cells, in particular, activity against human cancer cells.